UvrA is a component of the bacterial UvrABC DNA nucleotide excision repair system. The primary function of UvrA is to scan the DNA for lesions, which can vary greatly in their conformation and chemical structure, eventually initiating DNA repair. UvrA has a molecular weight of 104 kDa, is functional as a dimer and contains 2 zinc fingers, 1 helix-turn-helix motif and 2 ATP binding cassettes (ABC motifs). Its sequence homology to classical ABC transporters suggests common mechanisms and structural features for coupling ATP hydrolysis to mechanical actions. We have crystallized UvrA in the presence of ADP in spacegroup P212121 with unit cell dimensions of a = 152, b = 182, c = 225 E. The crystals grow to maximum dimensions of 2.5 x 1.0 x 0.03 mm and diffract to about 4 E at 130 K using rotating-anode X-ray generators and to about 3 E using synchrotron radiation (CHESS, ESRF).